ID D0JB68_BLASB Unreviewed; 268 AA.
AC D0JB68;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 13-SEP-2023, entry version 72.
DE RecName: Full=Diaminopimelate epimerase {ECO:0000256|HAMAP-Rule:MF_00197};
DE Short=DAP epimerase {ECO:0000256|HAMAP-Rule:MF_00197};
DE EC=5.1.1.7 {ECO:0000256|HAMAP-Rule:MF_00197};
DE AltName: Full=PLP-independent amino acid racemase {ECO:0000256|HAMAP-Rule:MF_00197};
GN Name=dapF {ECO:0000256|HAMAP-Rule:MF_00197,
GN ECO:0000313|EMBL:ACY40406.1};
GN OrderedLocusNames=BLBBGE_397 {ECO:0000313|EMBL:ACY40406.1};
OS Blattabacterium sp. subsp. Blattella germanica (strain Bge) (Blattella
OS germanica symbiotic bacterium).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Blattabacteriaceae; Blattabacterium.
OX NCBI_TaxID=331104 {ECO:0000313|EMBL:ACY40406.1, ECO:0000313|Proteomes:UP000002625};
RN [1] {ECO:0000313|EMBL:ACY40406.1, ECO:0000313|Proteomes:UP000002625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bge {ECO:0000313|Proteomes:UP000002625};
RX PubMed=19911043; DOI=10.1371/journal.pgen.1000721;
RA Lopez-Sanchez M.J., Neef A., Pereto J., Patino-Navarrete R., Pignatelli M.,
RA Latorre A., Moya A.;
RT "Evolutionary convergence and nitrogen metabolism in Blattabacterium strain
RT Bge, primary endosymbiont of the cockroach Blattella germanica.";
RL PLoS Genet. 5:E1000721-E1000721(2009).
CC -!- FUNCTION: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate
CC (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-
CC lysine and an essential component of the bacterial peptidoglycan.
CC {ECO:0000256|HAMAP-Rule:MF_00197}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S,6S)-2,6-diaminoheptanedioate = meso-2,6-
CC diaminoheptanedioate; Xref=Rhea:RHEA:15393, ChEBI:CHEBI:57609,
CC ChEBI:CHEBI:57791; EC=5.1.1.7; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00197};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
CC {ECO:0000256|HAMAP-Rule:MF_00197}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00197}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00197}.
CC -!- SIMILARITY: Belongs to the diaminopimelate epimerase family.
CC {ECO:0000256|ARBA:ARBA00010219, ECO:0000256|HAMAP-Rule:MF_00197}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00197}.
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DR EMBL; CP001487; ACY40406.1; -; Genomic_DNA.
DR RefSeq; WP_012840921.1; NC_013454.1.
DR AlphaFoldDB; D0JB68; -.
DR STRING; 331104.BLBBGE_397; -.
DR KEGG; bbl:BLBBGE_397; -.
DR eggNOG; COG0253; Bacteria.
DR HOGENOM; CLU_053306_3_2_10; -.
DR OMA; HVAMRVH; -.
DR OrthoDB; 9805408at2; -.
DR UniPathway; UPA00034; UER00025.
DR Proteomes; UP000002625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008837; F:diaminopimelate epimerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00197; DAP_epimerase; 1.
DR InterPro; IPR001653; DAP_epimerase_DapF.
DR NCBIfam; TIGR00652; DapF; 1.
DR PANTHER; PTHR31689:SF0; DIAMINOPIMELATE EPIMERASE; 1.
DR PANTHER; PTHR31689; DIAMINOPIMELATE EPIMERASE, CHLOROPLASTIC; 1.
DR Pfam; PF01678; DAP_epimerase; 2.
DR SUPFAM; SSF54506; Diaminopimelate epimerase-like; 2.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00197};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00197};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00197};
KW Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00197}.
FT ACT_SITE 73
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT ACT_SITE 206
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT BINDING 13
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT BINDING 74..75
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT BINDING 196..197
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT BINDING 207..208
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT SITE 146
FT /note="Could be important to modulate the pK values of the
FT two catalytic cysteine residues"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT SITE 196
FT /note="Could be important to modulate the pK values of the
FT two catalytic cysteine residues"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
SQ SEQUENCE 268 AA; 30775 MW; E7489160451A38E3 CRC64;
MKFNFFKYQG TGNDFILLDD RTKKIVKEYT ILKKLCNRHF GIGADGIILI QNDSKSDFYM
QYYNSDGKES TMCGNGGRCA IFFAKKLGIN KENKIHFRAI DGHHYGLIIK NEKNDKCLVS
INLINIQKNE IEIHPEHVFL NTGSPHHIIF VENIKEINVY EEGKKIRFRN PYLKKGVNVN
FVEILENKTL QVRTYERGVE NETLSCGTGV TASVIAAYET NRISSIEKIL VHTIGGKLWV
SLKETKNEYK DIYLTGSVQF IFQGCIFI
//